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PMID: 2022924 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Integrin-mediated localization of Bordetella pertussis within macrophages: role in pulmonary colonization.

The Journal of experimental medicine ·Vol. 173 ·No. 5 ·1991-05-01 ·Pages 1143-9

Saukkonen K, Cabellos C, Burroughs M, Prasad S, Tuomanen E

Abstract

The adherence of Bordetella pertussis to human respiratory cilia is critical to the pathogenesis of whooping cough but the significance of bacterial attachment to macrophages has not been determined. Adherence to cilia and macrophages is mediated by two large, nonfimbrial bacterial proteins, filamentous hemagglutinin (FHA), and pertussis toxin (PT). PT and FHA both recognize carbohydrates on cilia and macrophages; FHA also contains an Arg-Gly-Asp (RGD) sequence which promotes bacterial association with the macrophage integrin complement receptor 3 (CR3). We determined that virulent B. pertussis enter and survive in mammalian macrophages in vitro and that CR3 is important for this uptake process. We then determined the relative contribution of CR3 versus carbohydrate-dependent interactions to in vivo pulmonary colonization using a rabbit model. B. pertussis colonized the lung as two approximately equal populations, one extracellular population attached to ciliary and macrophage surface glycoconjugates and another population within pulmonary macrophages. Loss of the CR3 interaction, either by mutation of FHA or treatment with antibody to CR3, disrupted accumulation of viable intracellular bacteria but did not prevent lung pathology. In contrast, elimination of carbohydrate-bound bacteria, either by a competitive receptor analogue or an anti-receptor antibody, was sufficient to prevent pulmonary edema. We propose that CR3-dependent localization of B. pertussis within macrophages promotes persistence of bacteria in the lung without pulmonary injury. On the other hand, the presence of extracellular bacteria adherent to cilia and macrophages in carbohydrate-dependent interactions is associated with pulmonary pathology.

MeSH Terms
Adhesins, Bacterial Animals Bordetella pertussis/isolation & purification,pathogenicity,physiology Cilia/metabolism,microbiology,ultrastructure Hemagglutinins/metabolism,physiology Humans Integrins/metabolism,physiology Lung/microbiology,pathology,ultrastructure Macrophage-1 Antigen/metabolism,physiology Macrophages/metabolism,microbiology,ultrastructure Oligopeptides/metabolism,physiology Pertussis Toxin Rabbits Virulence Factors, Bordetella/metabolism,physiology
Chemicals
Adhesins, Bacterial Hemagglutinins Integrins Macrophage-1 Antigen Oligopeptides Virulence Factors, Bordetella filamentous hemagglutinin adhesin, Bordetella pertussis arginyl-glycyl-aspartic acid Pertussis Toxin
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Saukkonen K
Laboratory of Microbiology, Rockefeller University, New York, New York 10021.
Cabellos C
Burroughs M
Prasad S
Tuomanen E
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15 references, click to expand
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Article Info
Journal
The Journal of experimental medicine
Abbr.
J Exp Med
ISSN
0022-1007
Published
1991-05-01
Pages
1143-9
Language
English
Region
United States
NLM ID
2985109R
PMCID
PMC2118842
Subset
IM
Grants
NIAID NIH HHS · AI-RO1-23459 · United States
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